ArticleNucleic acids research2026
Zα and Zβ domains of ADAR1 and ZBP1 bind G-quadruplexes with nanomolar affinities, establishing Zβ as a G-quadruplex-specific domain.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structural and mechanistic basis of ADAR1-mediated RNA editing and immune regulation.Cell insight · 2026Review
- The Chromaverse Is Colored by Triplexes Formed Through the Interactions of Noncoding RNAs with HNPRNPU, TP53, AGO, REL Proteins, Intrinsically-Disordered Regions, and Flipons.International journal of molecular sciences · 2026Article
- ZBP1 contributes to IFN-β-induced PANoptosis-related skeletal muscle cell injury in dermatomyositis.Frontiers in immunology · 2026Article
- Control of Gene Expression by Proteins That Bind Many Alternative Nucleic Acid Structures Through the Same Domain.International journal of molecular sciences · 2025Article
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7 authors.
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Abstract
While it is well established that the Zα domains of ADAR1 and ZBP1 proteins bind Z-form-prone nucleic acids (Z-NAs), it has also been shown that the Zα domain of ADAR1 binds DNA G-quadruplexes (GQs). However, no binding partner of the structurally homologous Zβ domain of ADAR1 has been identified to date. Based on AlphaFold and molecular dynamics simulations, it has recently been suggested that Zβ of ADAR1 targets its substrate by recognizing GQs. Here, we provide the first experimental evidence for Zβ binding to select GQ RNA and DNA in vitro, with structural specificity and nanomolar affinity. We also demonstrate that the Zα domains of ZBP1 and ADAR1 bind to both DNA and RNA GQs with similar affinity. These findings extend the range of potential functional roles for these proteins and open new hypotheses for testing in cells.
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